Evidence map›Paper›PMID 28465431›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Vimentin fibers orient traction stress.

Nancy Costigliola, Liya Ding, Christoph J Burckhardt, Sangyoon J Han, Edgar Gutierrez, Andressa Mota, Alex Groisman, Timothy J Mitchison, Gaudenz Danuser

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
7.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

84 citing papers in PubMed, 143 citations in OpenAlex.

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  11. Vimentin - Force regulator in confined environments.Current opinion in cell biology · 2025
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24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Nancy CostigliolaDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Liya DingDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Christoph J BurckhardtDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Sangyoon J HanDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.ORCID 0000-0002-1384-665X
Edgar GutierrezDepartment of Physics, University of California, San Diego, La Jolla, CA 92093.
Andressa MotaDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115.
Alex GroismanDepartment of Physics, University of California, San Diego, La Jolla, CA 92093.
Timothy J MitchisonDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115.
Gaudenz DanuserDepartment of Cell Biology, Harvard Medical School, Boston, MA 02115; Gaudenz.Danuser@UTSouthwestern.edu.
Harvard University · USUniversity of California San Diego · US

Funding

Structural basis of the specific protein-protein interactions underlying IF assemP01GM096971 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI GOLDMAN, ROBERT D · 2011 to 2021
$16.8M
MICROTUBULE DYNAMICS AND MITOTIC MECHANISMR01GM039565 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI MITCHISON, TIMOTHY J · 1988 to 2018
$6.2M
NIGMS NIH HHS P01 GM096971NIGMS NIH HHS R01 GM039565
6 · The paper itself

Abstract

The intermediate filament vimentin is required for cells to transition from the epithelial state to the mesenchymal state and migrate as single cells; however, little is known about the specific role of vimentin in the regulation of mesenchymal migration. Vimentin is known to have a significantly greater ability to resist stress without breaking in vitro compared with actin or microtubules, and also to increase cell elasticity in vivo. Therefore, we hypothesized that the presence of vimentin could support the anisotropic mechanical strain of single-cell migration. To study this, we fluorescently labeled vimentin with an mEmerald tag using TALEN genome editing. We observed vimentin architecture in migrating human foreskin fibroblasts and found that network organization varied from long, linear bundles, or "fibers," to shorter fragments with a mesh-like organization. We developed image analysis tools employing steerable filtering and iterative graph matching to characterize the fibers embedded in the surrounding mesh. Vimentin fibers were aligned with fibroblast branching and migration direction. The presence of the vimentin network was correlated with 10-fold slower local actin retrograde flow rates, as well as spatial homogenization of actin-based forces transmitted to the substrate. Vimentin fibers coaligned with and were required for the anisotropic orientation of traction stresses. These results indicate that the vimentin network acts as a load-bearing superstructure capable of integrating and reorienting actin-based forces. We propose that vimentin's role in cell motility is to govern the alignment of traction stresses that permit single-cell migration.

Indexed as

ActinsAnimalsCell MovementCell PolarityElasticityEpithelial-Mesenchymal TransitionFibroblastsHumansIntermediate FilamentsMechanical PhenomenaMicrotubulesStress FibersVimentinWeight-BearingActinsVimentinfiber orientationintermediate filamentsmesenchymal migrationtraction stressvimentin

Identifiers

PMID28465431
PMCPMC5441818
OpenAlexW2611739609

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.